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- W1519158105 abstract "The purpose of this study was to investigate the regulatory protein (protein B) andcomponent interactions of soluble methane monooxygenase (sMMO). sMMO is amulti-component enzyme which catalyses the oxidation of methane to methanol. Itconsists of three proteins, a hydroxylase, a reductase and protein B (Colby andDalton, 1978). Protein B contains no metals, cofactors or prosthetic groups and has amolecular mass of 16 kDa. It has been shown that protein B is absolutely necessaryfor the hydroxylase activity of the sMMO complex and is a powerful regulator of theenzyme (Green and Dalton, 1985). It has also been found that 12 amino acids arecleaved from the N-terminus of protein B from Me. eapsulatus (Bath) to form aninactive truncate, known as protein B' and mutation of the Met12_Gly13 cleavage siteto Met12 -GIn I3 to give the single mutant protein G13Q, improved the stability of theprotein (Lloyd et al., 1997).Much of this work has concentrated on the study of the catalytic and regulatorysignificance of the 12 amino acids cleaved from protein B. Mc. eapsulatus (Bath)protein B appears to- cleave autocatalytically, generating the inactive protein B'truncate. The secondary structures of proteins B and B' were seen to be the same,although the overall structure was identified as differing slightly and protein B wasshown to be capable of existing in a monomer-dimer equilibrium, whereas protein B'was identified as existing in a monomer form. An homologous protein B from Ms.trichosporium OB3b, identified as being more a-helical in character, has been shownto be more stable than Mc. eapsulatus (Bath) protein B but still undergoes theinactivating cleavage reaction to form truncates, although the cleavage sites differbetween the two proteins.The construction, expression and purification of N-terminal truncates of Mc. capsulatus (Bath) protein B identified that the presence of thefirst 7 amino acids wasessential for protein B activity within the sMMO system and a decrease in specificactivity was observed as each amino acid from 1 to 7 was lost. Upon loss of the 7thamino acid, tyrosine, the truncate protein was observed to be totally inactive and alsomuch more prone to cleavage, but unchanged in terms of secondary structure.Protein concentration was observed as having an effect on the stability of Mc.capsulatus (Bath) protein B and, the single mutant G13Q, with increasedconcentrations improving stability. This effect was not observed for the doublemutant MI2A:G13Q, although it was shown to be more stable than the otherproteins under more dilute conditions. The addition of a magnesium salt alsoimproved the stability of protein B.Studies into the interactions of protein B with the other proteins within the sMMOcomplex have also been performed. Evidence that the hydroxylase undergoes a largeconformational change upon the binding of the reductase and protein B has beenobtained and modelled to suggest that one trimer of the hydroxylase dimer rotates by1800 relative to the other upon complex formation. It also showed the sMMOcomplex to form in a stoichiometry of 1:2:2 hydroxylase:reductase:protein B. Otherdata suggest that -sMMO component binding occurs on only one trimer of thehydroxylase dimer under different conditions." @default.
- W1519158105 created "2016-06-24" @default.
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- W1519158105 date "2000-09-01" @default.
- W1519158105 modified "2023-09-24" @default.
- W1519158105 title "The regulatory protein and component interactions of soluble methane monooxygenase" @default.
- W1519158105 hasPublicationYear "2000" @default.
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